scholarly journals Molecular characterization and functional expression of squid retinal-binding protein. A novel species of hydrophobic ligand-binding protein.

1994 ◽  
Vol 269 (5) ◽  
pp. 3838-3845
Author(s):  
K. Ozaki ◽  
A. Terakita ◽  
M. Ozaki ◽  
R. Hara ◽  
T. Hara ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Molecular Characterization ◽  
Novel Species ◽  
Binding Protein ◽  
Protein A ◽  
Functional Expression ◽  
Hydrophobic Ligand

scholarly journals Identification of Discrete Domains within Gonococcal Transferrin-Binding Protein A That Are Necessary for Ligand Binding and Iron Uptake Functions

2000 ◽  
Vol 68 (12) ◽  
pp. 6988-6996 ◽  
Author(s):  
Ian C. Boulton ◽  
Mary Kate Yost ◽  
James E. Anderson ◽  
Cynthia Nau Cornelissen
Keyword(s):  
Ligand Binding ◽  
Iron Uptake ◽  
Binding Protein ◽  
Protein A ◽  
Ligand Interaction ◽  
Whole Cells ◽  
Affinity Ligand ◽  
Discrete Domains ◽  
Transferrin Binding Proteins

ABSTRACT The availability of free iron in vivo is strictly limited, in part by the iron-binding protein transferrin. The pathogenicNeisseria spp. can sequester iron from this protein, dependent upon two iron-repressible, transferrin-binding proteins (TbpA and TbpB). TbpA is a TonB-dependent, integral, outer membrane protein that may form a β-barrel exposing multiple surface loops, some of which are likely to contain ligand-binding motifs. In this study we propose a topological model of gonococcal TbpA and then test some of the hypotheses set forth by the model by individually deleting three putative loops (designated loops 4, 5, and 8). Each mutant TbpA could be expressed without toxicity and was surface exposed as assessed by immunoblotting, transferrin binding, and protease accessibility. Deletion of loop 4 or loop 5 abolished transferrin binding to whole cells in solid- and liquid-phase assays, while deletion of loop 8 decreased the affinity of the receptor for transferrin without affecting the copy number. Strains expressing any of the three mutated TbpAs were incapable of growth on transferrin as a sole iron source. These data implicate putative loops 4 and 5 as critical determinants for receptor function and transferrin-iron uptake by gonococcal TbpA. The phenotype of the ΔL8TbpA mutant suggests that high-affinity ligand interaction is required for transferrin-iron internalization.

A hydrophobic ligand-binding protein of theTaenia solium metacestode mediates uptake of the host lipid: Implication for the maintenance of parasitic cellular homeostasis

PROTEOMICS ◽  
2007 ◽  
Vol 7 (21) ◽  
pp. 4016-4030 ◽  
Author(s):  
Eung-Goo Lee ◽  
Seon-Hee Kim ◽  
Young-An Bae ◽  
Joon-Yong Chung ◽  
Myungkoo Suh ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Cellular Homeostasis ◽  
Hydrophobic Ligand

Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface

2015 ◽  
Vol 93 ◽  
pp. 17-23 ◽  
Author(s):  
Valeria Silva-Álvarez ◽  
Ana Maite Folle ◽  
Ana Lía Ramos ◽  
Fernando Zamarreño ◽  
Marcelo D. Costabel ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Echinococcus Granulosus ◽  
Binding Protein ◽  
Antigen B ◽  
Host Parasite ◽  
Hydrophobic Ligand

scholarly journals Ligand-Binding Properties of the Carboxyl-Terminal Repeat Domain of Streptococcus mutans Glucan-Binding Protein A

2000 ◽  
Vol 182 (3) ◽  
pp. 728-733 ◽  
Author(s):  
Wolfgang Haas ◽  
Jeffrey A. Banas
Keyword(s):  
Ligand Binding ◽  
Streptococcus Mutans ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Protein A ◽  
Binding Constants ◽  
Water Soluble ◽  
Soluble Form ◽  
Tooth Surface ◽  
Carboxyl Terminal

ABSTRACT Streptococcus mutans glucan-binding protein A (GbpA) has sequence similarity in its carboxyl-terminal domain with glucosyltransferases (GTFs), the enzymes responsible for catalyzing the synthesis of the glucans to which GbpA and GTFs can bind and which promote S. mutans attachment to and accumulation on the tooth surface. It was predicted that this C-terminal region, comprised of what have been termed YG repeats, represents the GbpA glucan-binding domain (GBD). In an effort to test this hypothesis and to quantitate the ligand-binding specificities of the GbpA GBD, several fusion proteins were generated and tested by affinity electrophoresis or by precipitation of protein-ligand complexes, allowing the determination of binding constants. It was determined that the 16 YG repeats in GbpA comprise its GBD and that GbpA has a greater affinity for dextran (a water-soluble form of glucan) than for mutan (a water-insoluble form of glucan). Placement of the GBD at the carboxyl terminus was necessary for maximum glucan binding, and deletion of as few as two YG repeats from either end of the GBD reduced the affinity for dextran by over 10-fold. Interestingly, the binding constant of GbpA for dextran was 34-fold higher than that calculated for the GBDs of two S. mutans GTFs, one of which catalyzes the synthesis of water-soluble glucan and the other of which catalyzes the synthesis of water-insoluble glucan.

A new diagnostic tool for neurocysticercosis is a member of a cestode specific hydrophobic ligand binding protein family 1

FEBS Letters ◽  
2000 ◽  
Vol 487 (2) ◽  
pp. 181-184 ◽  
Author(s):  
Nahid Saghir ◽  
Phillip J. Conde ◽  
Peter M. Brophy ◽  
John Barrett
Keyword(s):  
Ligand Binding ◽  
Diagnostic Tool ◽  
Binding Protein ◽  
Protein Family ◽  
Hydrophobic Ligand
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